
FREE
for Members
Chemical Biology Discussion Group Year-End Symposium
Wednesday, June 5, 2013
Chemical biology is a diverse and dynamic field involving chemical approaches to studying and manipulating biological systems. The goal of the Academy's Chemical Biology Discussion Group meetings is to enhance interactions among local-area laboratories working in chemical biology and to feature forefront research in chemical biology to the wider community. The meeting traditionally covers a range of current topics in chemical biology, including chemical probe development, organic synthesis, biosynthesis, protein engineering, nanotechnology, and drug discovery. The annual year-end meeting features distinguished keynote speaker Professor Alanna Schepartz of Yale University. This will be followed by shorter, cutting-edge talks by graduate students and postdoctoral fellows selected from participating tristate-area institutions, and a poster session.
*Reception to follow.
Registration Pricing
Member | $0 |
Student/Postdoc Member | $0 |
Nonmember | $40 |
Nonmember (Student / Postdoc / Resident / Fellow) | $20 |
The Chemical Biology Discussion Group is proudly supported by 
Mission Partner support for the Frontiers of Science program provided by 
Agenda
* Presentation times are subject to change.
Wednesday, June 5, 2013 | |
11:30 AM | Registration and Poster Set-up |
12:00 PM | Welcome and Introduction |
12:10 PM | Bioorthogonal Labeling of Substrates of Type I Protein Arginine Methyltransferases (PRMTS) by Engineered Enzymes |
12:30 PM | The Design and Characterization of Helical Protein Fibers |
12:50 PM | The Ultrafast Split Inteins and their Use in Modern Protein Semisynthesis |
1:10 PM | Aldehyde Capture Ligation for Synthesis of Peptides and Proteins |
1:30 PM | Coffee Break and Poster Session |
2:30 PM | RNA Mimics of Red Fluorescent Protein |
2:50 PM | Structure of the Arginine Methyltransferase PRMT5-MEP50 Reveals a Mechanism for Substrate Specificity |
3:10 PM | Keynote Presentation: Visualizing Information Transfer through the Plasma Membrane |
4:10 PM | Networking Reception and Poster Session |
5:00 PM | Close |
Speakers
Organizers
Akira Kawamura, PhD
Hunter College, CUNY
Akira Kawamura received his B.Sc. and M.Sc. degrees in Organic Chemistry at the University of Tokyo. Attracted to the magnetic character of Professor Koji Nakanishi, Akira crossed the Pacific Ocean in 1994 to join the chemistry Ph.D. program at Columbia Univeristy. He received his Ph.D. under the direction of Koji Nakanishi and Nina Berova in 1999.
Before joining Hunter College, he spent his postdoctoral stint in the group of Peter G. Schultz at the Scripps Research Institute (1999-2002). Akira is currently an associate professor of chemistry at Hunter College, conducting research in bioorganic and natural products chemistry.
Jonathan Lai, PhD
Albert Einstein College of Medicine
Jon Lai is Associate Professor of Biochemistry at the Albert Einstein College of Medicine, Bronx, NY. His group's principal interests are in peptide and protein engineering strategies for biomedical applications. A major recent focus has been the development of antibody phage display technologies, and their application to a wide variety of targets such as viruses and oligosaccharides. Another area of interest is understanding viral glycoprotein function using a combination of structural and mutagenesis studies. Dr. Lai received his B. Sc. (Hons.) in Biochemistry from Queen's University in Kingston, Ontario, Canada in 1999, then his Ph. D. in Biophysics and Chemistry from the University of Wisconsin (Madison) in 2004 where he studied peptide structure and function. From 2004-2007 he performed post-doctoral studies at Harvard Medical School in enzymology and X-ray crystallography before beginning his independent position at Einstein.
Jennifer Henry, PhD
The New York Academy of Sciences
Keynote Speaker
Alanna Schepartz, PhD
Yale University
Alanna Schepartz, PhD, is the Milton Harris '29 PhD Professor of Chemistry and Professor of Molecular, Cellular, and Developmental Biology at Yale University.
Professor Schepartz was born on January 9, 1962 in New York City and was graduated from Forest Hills High School in 1978. After receiving a BS degree in Chemistry from the State University of New York–Albany in 1982, Alanna carried out graduate work at Columbia University under the supervision of Ronald Breslow. Following postdoctoral work with Peter Dervan at the California Institute of Technology, she joined the faculty at Yale University in July of 1988. She was promoted to Associate Professor in 1992, to Full Professor with tenure in 1995, and was named the Milton Harris, '29 PhD Professor of Chemistry in 2000. From 2002–2007, she held a Howard Hughes Medical Institute Professorship. In 2011, she was appointed as the Director of the Yale Chemical Biology Institute.
Alanna Schepartz is well known for the creative application of chemical synthesis and principles to understand and control biological recognition and function. Her research has contributed to and shaped thinking in multiple areas, including the molecular mechanisms of protein–DNA recognition and transcriptional activation; protein design and engineering and their application to synthetic biology; and the mechanisms by which chemical information is trafficked across biological compartments. She is also widely recognized for her design of the first and only example of protein-like architecture that lacks even a single α-amino acid.
Alanna Schepartz has received a number of awards for her work, including a David and Lucile Packard Foundation Fellowship (1990), a N.S.F. Presidential Young Investigator Award (1991), a Camille and Henry Dreyfus Teacher–Scholar Award (1993), an Alfred P. Sloan Research Fellowship (1994), an A.C.S. Arthur C. Cope Scholar Award (1995), the A.C.S. Eli Lilly Award in Biological Chemistry (1997), the Dylan Hixon '88 Award for Teaching Excellence in the Natural Sciences (1999), the Agnes Fay Morgan Research Award (2002), the Frank H. Westheimer Prize Medal (2008), the ACS Chemical Biology Prize & Prize Lecture (2010), for which she was the inaugural recipient, the Alexander M. Cruickshank Prize (2010) and the Ronald Breslow Award for Achievement in Biomimetic Chemistry (2012). In 2010, Schepartz was elected as a Fellow of both the American Academy of Arts & Sciences and the American Chemical Society. Since 2005, she has served the chemical biology community as an Associate Editor of the Journal of the American Chemical Society.
Speakers
Han Guo
Luo lab, Memorial Sloan–Kettering Cancer Center
Han Guo is a fourth year graduate student from the Tri-Institutional Training Program in Chemical Biology (TPCB). Born in China, he came to the U.S. in 2005 to attend Bowdoin College. During his undergraduate study, Mr. Guo worked in Dr. Danielle Dube’s lab and developed a strong interest in Chemical Biology from his project of developing chemical tools to target Helicobacter pylori glycosylation through the synthesis of azide-containing glycans, which was supported by the HHMI summer fellowship. In 2009, he received his B.A. in Biochemistry and German, and became a member of the Phi Beta Kappa Society. Mr. Guo joined Dr. Minkui Luo’s lab at Memorial Sloan Kettering Cancer Institute in 2010 and is currently working on the development of Bioorthogonal Profiling of Protein Methylation (BPPM) to understand the biological functions of type I Protein Arginine N-methyltransferases (PRMTs) by identifying their cellular substrates.
Rudy Jacquet
Montclare lab, NYU–Poly
Rudy Jacquet is a Master’s student in biotechnology at NYU-POLY. My goal is to one day contribute to the pharmaceutical and biotech industry. Having obtained my bachelor’s degree in biology at Lehman College and the opportunity right after to conduct research at University of Michigan, my desire for scientific research goes as back as I can remember. Now, moving forward, this desire has led me to the exploration of new research area such as protein engineering. Whereas before I was exposed to biomedical research, currently I am learning the great potential that research in the material sciences hold for the advancement of our society. Thus, as the son of Haitian immigrants and the first of my family to graduate college, I have cherished the opportunities granted so far to me. With each new stride and exploration I have made, beginning with my fascination of the sciences from my classes to working at the bench, my motivation toward scientific research grew. I am thankful for having the opportunity to contribute to scientific research. A field that is highly interesting, valuable and grand.
Neel Shah
Muir lab, Princeton University
Neel Shah received his B.S. in Chemistry in 2008 from New York University. At NYU, he worked in Professor Kent Kirshenbaum’s lab and developed a novel method for constraining the backbone conformations of a class of peptidomimetic oligomers. After obtaining his undergraduate degree, he began his graduate studies at The Rockefeller University under the advisement of Professor Tom Muir. Neel moved with the Muir lab to Princeton University in 2011 and is currently carrying out his doctoral research on the biochemical and biophysical characterization of naturally split inteins.
Monika Raj, PhD
Arora lab, NYU
Monika Raj is a postdoc at New York University in the Arora Lab. Born in India; she completed her Phd in field of Organocatalysts from Indian Institute of Technology, one of the premier institutes in India. Monika spent a brief amount of time as a postdoc at the University of Pennsylvania with Prof. Barry Cooperman. At UPenn, her work was focused on developing the protein sequence monitoring technology. Through this effort, she completed determining the mechanism and distribution of fluorescent labeling of tRNA. Currently, in the Arora lab at NYU, Monika is working towards the development of new methodologies and auxiliaries to carry out ligation of peptides, proteins and peptidiomimetics.
Wenjiao Song, PhD
Jaffrey lab, Weill Medical College, Cornell University
Wenjiao Song joined Dr Jaffrey’s lab at Weill Cornell Medical College as a postdoctoral associate in July, 2010. Since coming to Dr Jaffrey’s lab, she has developed a strategy to make RNAs that recognize specific proteins and undergo conformational changes that result in the RNAs becoming fluorescent. This work is currently under review at Nature Methods. She currently is developing a new class of RNA molecules which bind to and activate the fluorescence of fluorophores that resembled those that naturally occur in red fluorescent proteins found in coral. Before joining Dr Jaffrey’s laboratory she has an extremely successful graduate experience in the laboratory of Qing Lin at SUNY Buffalo, where she focused on new methods for protein modification and conjugating proteins with fluorescent dyes in living cells. Wenjiao’s work led to numerous peer-reviewed papers, including four first-author papers in journals such as the Journal of the American Chemical Society, Angew. Chemie, and ACS Chemical Biology.
Carola Wilczek, PhD
Shechter lab, Albert Einstein College of Medicine
Carola Wilczek received her diploma (master) in chemistry from the Westfaelische Wilhelms-University (WWU) in Muenster, Germany in 2005. She did her PhD at the WWU in the laboratory of Karl-Heinz Klempnauer studying changes in chromatin structure caused by the transcription factor and oncogene c-Myb. Carola’s postdoctoral work at Albert Einstein College of Medicine in David Shechter’s laboratory focuses on understanding the mechanism of the essential histone arginine methyltransferase complex PRMT5-MEP50.
Sponsors
Promotional Partner
The Chemical Biology Discussion Group is proudly supported by 
Mission Partner support for the Frontiers of Science program provided by 
Abstracts
Bioorthogonal Labeling of Substrates of Type I Protein Arginine methyltransferases (PRMTs) by engineered enzymes
Han Guo, Molecular Pharmacology and Chemistry Program & Tri-Institutional Training Program in Chemical Biology, Memorial Sloan Kettering Cancer Institute
Co-Author: Minkui Luo, PhD, Molecular Pharmacology and Chemistry Program, Memorial Sloan Kettering Cancer Institute, and Tri-Institutional Training Program in Chemical Biology, Memorial Sloan Kettering Cancer Institute
The Design and Characterization of Helical Protein Fibers
Rudy Jacquet, Department of Chemical and Biological Engineering, Polytechnic Institute of New York University
Co-Authors: Jasmin Hume, Jennifer Sun, Jin Kim Montclare, Department of Chemical and Biological Engineering, Polytechnic Institute of New York University
Ultrafast Split Inteins and their use in Modern Protein Semisynthesis
Neel H. Shah, Princeton University
Co-Authors: Miquel Vila-Perelló, Zhihua Liu, Tom W. Muir, Princeton University
Aldehyde Capture Ligation for Synthesis of Peptides and Proteins
Monika Raj, Department of Chemistry, New York University
Co-Authors: Huabin Wu, Paramjit S. Arora, Department of Chemistry, New York University
References:
1Dawson, P. E.; Muir, T. W.; Clark-Lewis, I.; Kent, S. B. Science 1994, 266, 776-779.
2 (a) Shang, S.; Tan, Z.; Dong, S.; Danishefsky, S. J. J. Am. Chem. Soc., 2011, 133, 10784–10786. (b) Yang, R. L.; Pasunooti, K. K.; Li, F. P.; Liu, X. W.; Liu, C. F. J. Am. Chem. Soc. 2009, 131, 13592-13597. (c) Harpaz, Z.; Siman, P.; Kumar, K. S. A.; Brik, A. Chem. Bio. Chem. 2010, 11,1232–1235. (d) Chen, J.; Wang, P.; Zhu, J. L.; Wan, Q.; Danishefsky, S. J. Tetrahedron 2010, 66, 2277-2280.
RNA Mimics of Red Fluorescent Protein
Wenjiao Song, PhD, Weill Medical College, Cornell University
Co-Author: Samie R. Jaffrey, MD, PhD, Weill Medical College, Cornell University
Structure of the Arginine Methyltransferase PRMT5-MEP50 Reveals a Mechanism for Substrate Specificity
Carola Wilczek, Department of Biochemistry, Albert Einstein College of Medicine, Yeshiva University*
Histone peptide arrays and solution assays demonstrate that PRMT5-MEP50 activity is inhibited by substrate phosphorylation and enhanced by substrate acetylation. PRMT5-MEP50 methylates H2A/H2B dimers, H3/H4 tetramers, and octamers, but cannot methylate nucleosomes. Electron microscopy showed substrate density centered on MEP50. These data suggest a mechanism in which MEP50 binds substrate and presents it to the cross-dimer PRMT5 to align the substrate arginine in the active site, modulated by substrate post-translational modifications.
Co-Authors: Meng-Chiao Ho2*, Jeffrey B. Bonnano1, Li Xing3, Janina Seznec4, Tsutomu Matsui5, Lester G. Carter5, Takashi Onikubo1, P. Rajesh Kumar1, Man K. Chan1, Michael Brenowitz2, R. Holland Cheng3, Ulf Reimer4, Steven C. Almo1, and David Shechter1
1Department of Biochemistry, Albert Einstein College of Medicine, Yeshiva University
2Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan
3Department of Molecular and Cellular Biology, University of California, Davis
4JPT Peptide Technologies, Berlin, Germany
5Stanford Synchroton Radiation Lightsource, SLAC National Accelerator Laboratory, California
*contributed equally
Visualizing Information Transfer Through the Plasma Membrane
Alanna Schepartz, PhD, Department of Chemistry, Yale University
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